PMID- 17451749
OWN - NLM
STAT- MEDLINE
DCOM- 20070813
LR  - 20070611
IS  - 0022-5193 (Print)
IS  - 0022-5193 (Linking)
VI  - 247
IP  - 2
DP  - 2007 Jul 21
TI  - Exploring the role of cation-pi interactions in glycoproteins lipid-binding 
      proteins and RNA-binding proteins.
PG  - 346-53
AB  - We have analyzed and compared the influence of cation-pi interactions in 
      glycoproteins (GPs), lipid-binding proteins (LBPs) and RNA-binding proteins 
      (RBPs) in this study. We observed that all the proteins included in the study had 
      profound cation-pi interactions. There is an average of one energetically 
      significant cation-pi interaction for every 71 residues in GPs, for every 58 
      residues in LBPs and for every 64 residues in RBPs. Long-range contacts are 
      predominant in all the three types of proteins studied. The pair-wise cation-pi 
      interaction energy between the positively charged and aromatic residues shows 
      that Arg-Trp pair energy was the strongest among all six possible pairs in all 
      the three types of proteins studied. There were considerable differences in the 
      preference of cation-pi interacting residues to different secondary structure 
      elements and ASA and these might contribute to differences in biochemical 
      functions of GPs, LBPs and RBPs. It was interesting to note that all the five 
      residues involved in cation-pi interactions were found to have stabilization 
      centers in GPs, LBPs and RBPs. Majority of the cation-pi interacting residues 
      investigated in the present study had a conservation score of 6, the cutoff value 
      used to identify the stabilizing residues. A small percentage of cation-pi 
      interacting residues were also present as stabilizing residues. The cation-pi 
      interaction-forming residues play an important role in the structural stability 
      of in GPs, LBPs and RBPs. The results obtained in this study will be helpful in 
      further understanding the stability, specificity and differences in the 
      biochemical functions of GPs, LBPs and RBPs.
FAU - Anbarasu, Anand
AU  - Anbarasu A
AD  - School of Bio-Technology Chemical and Bio-Medical Engineering, VIT University, 
      Vellore 632014, India.
FAU - Sethumadhavan, Rao
AU  - Sethumadhavan R
LA  - eng
PT  - Journal Article
DEP - 20070312
PL  - England
TA  - J Theor Biol
JT  - Journal of theoretical biology
JID - 0376342
RN  - 0 (Cations)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (RNA-Binding Proteins)
SB  - IM
MH  - Animals
MH  - Cations/metabolism
MH  - Fatty Acid-Binding Proteins/*metabolism
MH  - Glycoproteins/*metabolism
MH  - Protein Structure, Secondary
MH  - RNA-Binding Proteins/*metabolism
EDAT- 2007/04/25 09:00
MHDA- 2007/08/19 09:00
CRDT- 2007/04/25 09:00
PHST- 2006/11/07 00:00 [received]
PHST- 2007/01/30 00:00 [revised]
PHST- 2007/02/27 00:00 [accepted]
PHST- 2007/04/25 09:00 [pubmed]
PHST- 2007/08/19 09:00 [medline]
PHST- 2007/04/25 09:00 [entrez]
AID - S0022-5193(07)00094-X [pii]
AID - 10.1016/j.jtbi.2007.02.018 [doi]
PST - ppublish
SO  - J Theor Biol. 2007 Jul 21;247(2):346-53. doi: 10.1016/j.jtbi.2007.02.018. Epub 
      2007 Mar 12.